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Analyzing conformational changes in single FRET-labeled A1 parts of archaeal A1AO-ATP synthase
Author(s): Hendrik Sielaff; Dhirendra Singh; Gerhard Grüber; Michael Börsch
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Paper Abstract

ATP synthases utilize a proton motive force to synthesize ATP. In reverse, these membrane-embedded enzymes can also hydrolyze ATP to pump protons over the membrane. To prevent wasteful ATP hydrolysis, distinct control mechanisms exist for ATP synthases in bacteria, archaea, chloroplasts and mitochondria. Single-molecule Förster resonance energy transfer (smFRET) demonstrated that the C-terminus of the rotary subunit ε in the Escherichia coli enzyme changes its conformation to block ATP hydrolysis. Previously, we investigate the related conformational changes of subunit F of the A1AO-ATP synthase from the archaeon Methanosarcina mazei Gö1. Here, we analyzed the lifetimes of fluorescence donor and acceptor dyes to distinguish between smFRET signals of conformational changes and potential artefacts.

Paper Details

Date Published: 20 February 2018
PDF: 12 pages
Proc. SPIE 10500, Single Molecule Spectroscopy and Superresolution Imaging XI, 1050007 (20 February 2018); doi: 10.1117/12.2286785
Show Author Affiliations
Hendrik Sielaff, Universitätsklinikum Jena (Germany)
Nanyang Technological Univ. (Singapore)
Dhirendra Singh, Nanyang Technological Univ. (Singapore)
Gerhard Grüber, Nanyang Technological Univ. (Singapore)
Michael Börsch, Universitätsklinikum Jena (Germany)


Published in SPIE Proceedings Vol. 10500:
Single Molecule Spectroscopy and Superresolution Imaging XI
Jörg Enderlein; Ingo Gregor; Zygmunt Karol Gryczynski; Rainer Erdmann; Felix Koberling, Editor(s)

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